ID   TYPH_MYCPN              Reviewed;         421 AA.
AC   P75052;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Thymidine phosphorylase;
DE            EC=2.4.2.4;
DE   AltName: Full=TdRPase;
GN   Name=deoA; OrderedLocusNames=MPN_064; ORFNames=MP090;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
CC   -!- FUNCTION: The enzymes which catalyze the reversible phosphorolysis of
CC       pyrimidine nucleosides are involved in the degradation of these
CC       compounds and in their utilization as carbon and energy sources, or in
CC       the rescue of pyrimidine bases for nucleotide synthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate +
CC         thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.4;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000305}.
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DR   EMBL; U00089; AAB95738.1; -; Genomic_DNA.
DR   PIR; S73416; S73416.
DR   RefSeq; NP_109752.1; NC_000912.1.
DR   RefSeq; WP_010874421.1; NC_000912.1.
DR   AlphaFoldDB; P75052; -.
DR   SMR; P75052; -.
DR   IntAct; P75052; 1.
DR   STRING; 272634.MPN_064; -.
DR   EnsemblBacteria; AAB95738; AAB95738; MPN_064.
DR   KEGG; mpn:MPN_064; -.
DR   PATRIC; fig|272634.6.peg.65; -.
DR   HOGENOM; CLU_025040_0_1_14; -.
DR   OMA; DVWRRMI; -.
DR   BioCyc; MPNE272634:G1GJ3-100-MON; -.
DR   BRENDA; 2.4.2.4; 3534.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR   GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro.
DR   GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1030.10; -; 1.
DR   Gene3D; 3.90.1170.30; -; 1.
DR   InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR   InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR   InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR   InterPro; IPR035902; Nuc_phospho_transferase.
DR   InterPro; IPR036566; PYNP-like_C_sf.
DR   InterPro; IPR013102; PYNP_C.
DR   InterPro; IPR018090; Pyrmidine_PPas_bac/euk.
DR   InterPro; IPR017872; Pyrmidine_PPase_CS.
DR   InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR   PANTHER; PTHR10515; PTHR10515; 1.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   Pfam; PF07831; PYNP_C; 1.
DR   PIRSF; PIRSF000478; TP_PyNP; 1.
DR   SMART; SM00941; PYNP_C; 1.
DR   SUPFAM; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   SUPFAM; SSF54680; SSF54680; 1.
DR   TIGRFAMs; TIGR02644; Y_phosphoryl; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..421
FT                   /note="Thymidine phosphorylase"
FT                   /id="PRO_0000059081"
SQ   SEQUENCE   421 AA;  46628 MW;  E29DBF93C6D8549F CRC64;
     MNIVNLISKK QRGKALTETE INWFVHSVNN KSLADYQVSA FLMAVWFQGM NSKELFCLTK
     AMVKSGESLH FNHHSKLSVD KHSTGGIGDK VSIALIPILT ALDYSVAKLS GRGLGYTGGT
     IDKLEAVGVK TDFTPTEAQN LLDQNDCFII GQSEGIAPVD KVLYALRDTT ATVDSLPLIA
     SSVMSKKLAI NNDYIFIDLK YGKGAFCKTK TMAKELAQYM YSIAKQFKRK LYIKLSDMNQ
     VLGKTIGNAL EVLEVVHFLK RNWTEVGADF IQLMEQIVTE ILIETKRAPN KRAAVALYHA
     TLEGEKPWQR FLKFIELQGS SWERFLDLKE LFNPQYKAPV LASQSGTLSY TSPVDLAMVS
     ISLGAGRMVK TDLIDPMAGI KLVKQANEVV KAGDTVLELY SSKPITPAHI EAAQHTIIIK
     Q